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Q8WWW0

- RASF5_HUMAN

UniProt

Q8WWW0 - RASF5_HUMAN

Protein

Ras association domain-containing protein 5

Gene

RASSF5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Potential tumor suppressor. Seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. Isoform 2 stimulates lymphocyte polarization and the patch-like distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to ICAM1. Together with RAP1A may participate in regulation of microtubule growth. The association of isoform 2 with activated RAP1A is required for directional movement of endothelial cells during wound healing. May be involved in regulation of Ras apoptotic function. The RASSF5-STK4/MST1 complex may mediate HRAS and KRAS induced apoptosis.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri122 – 17049Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. intracellular signal transduction Source: InterPro
    3. positive regulation of protein ubiquitination Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ8WWW0.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras association domain-containing protein 5
    Alternative name(s):
    New ras effector 1
    Regulator for cell adhesion and polarization enriched in lymphoid tissues
    Short name:
    RAPL
    Gene namesi
    Name:RASSF5
    Synonyms:NORE1, RAPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17609. RASSF5.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton
    Note: Isoform 2 is mainly located in the perinuclear region of unstimulated primary T-cells. Upon stimulation translocates to the leading edge and colocalizes with ITGAL/LFA-1 in the peripheral zone of the immunological synapse. Isoform 2 is localized to growing microtubules in vascular endothelial cells and is dissociated from microtubules by activated RAP1A.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. microtubule Source: UniProtKB-KW
    3. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA134958571.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Ras association domain-containing protein 5PRO_0000240401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei352 – 3521Phosphothreonine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8WWW0.
    PaxDbiQ8WWW0.
    PRIDEiQ8WWW0.

    PTM databases

    PhosphoSiteiQ8WWW0.

    Expressioni

    Tissue specificityi

    Widely expressed. Frequently down-regulated in lung tumor cell lines and primary lung tumors.2 Publications

    Gene expression databases

    ArrayExpressiQ8WWW0.
    BgeeiQ8WWW0.
    CleanExiHS_RASSF5.
    GenevestigatoriQ8WWW0.

    Organism-specific databases

    HPAiCAB022664.

    Interactioni

    Subunit structurei

    Interacts directly with activated HRAS; a RASSF5-STK4/MST1 complex probably associates with activated HRAS. Interacts with KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS, RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1 isoform A. The RSSF1 isoform A-RSSF5 heterodimer probably mediates the association of RSSF1 with HRAS By similarity. Isoform 2 interacts with activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4/MST1 autoactivation.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GABARAPO951662EBI-367390,EBI-712001
    GABARAPL1Q9H0R82EBI-367390,EBI-746969
    GABARAPL2P605202EBI-367390,EBI-720116
    HRASP011122EBI-367390,EBI-350145
    MAP1LC3BQ9GZQ85EBI-367390,EBI-373144
    MAP1LC3CQ9BXW42EBI-367390,EBI-2603996
    RAP1AP628343EBI-960502,EBI-491414
    STK3Q131887EBI-367390,EBI-992580
    STK4Q130437EBI-367390,EBI-367376

    Protein-protein interaction databases

    BioGridi123689. 29 interactions.
    DIPiDIP-32490N.
    IntActiQ8WWW0. 30 interactions.
    STRINGi9606.ENSP00000347443.

    Structurei

    Secondary structure

    1
    418
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi369 – 3713
    Helixi374 – 41037

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4LGDX-ray3.05E/F/G/H365-413[»]
    ProteinModelPortaliQ8WWW0.
    SMRiQ8WWW0. Positions 113-170, 205-362, 366-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini274 – 36491Ras-associatingPROSITE-ProRule annotationAdd
    BLAST
    Domaini366 – 41348SARAHPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 Ras-associating domain.PROSITE-ProRule annotation
    Contains 1 SARAH domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri122 – 17049Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG308852.
    HOGENOMiHOG000013025.
    HOVERGENiHBG054362.
    InParanoidiQ8WWW0.
    KOiK08015.
    OMAiNCLLMKL.
    OrthoDBiEOG7TF796.
    PhylomeDBiQ8WWW0.
    TreeFamiTF319243.

    Family and domain databases

    InterProiIPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000159. Ras-assoc.
    IPR011524. SARAH_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00130. C1_1. 1 hit.
    PF00788. RA. 1 hit.
    [Graphical view]
    SMARTiSM00109. C1. 1 hit.
    SM00314. RA. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50200. RA. 1 hit.
    PS50951. SARAH. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WWW0-1) [UniParc]FASTAAdd to Basket

    Also known as: A, NORE1A

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAMASPAIGQ RPYPLLLDPE PPRYLQSLSG PELPPPPPDR SSRLCVPAPL    50
    STAPGAREGR SARRAARGNL EPPPRASRPA RPLRPGLQQR LRRRPGAPRP 100
    RDVRSIFEQP QDPRVPAERG EGHCFAELVL PGGPGWCDLC GREVLRQALR 150
    CTNCKFTCHP ECRSLIQLDC SQQEGLSRDR PSPESTLTVT FSQNVCKPVE 200
    ETQRPPTLQE IKQKIDSYNT REKNCLGMKL SEDGTYTGFI KVHLKLRRPV 250
    TVPAGIRPQS IYDAIKEVNL AATTDKRTSF YLPLDAIKQL HISSTTTVSE 300
    VIQGLLKKFM VVDNPQKFAL FKRIHKDGQV LFQKLSIADR PLYLRLLAGP 350
    DTEVLSFVLK ENETGEVEWD AFSIPELQNF LTILEKEEQD KIQQVQKKYD 400
    KFRQKLEEAL RESQGKPG 418
    Length:418
    Mass (Da):47,090
    Last modified:March 1, 2002 - v1
    Checksum:i4AFBC69B1325CC9E
    GO
    Isoform 2 (identifier: Q8WWW0-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         1-153: Missing.
         154-193: CKFTCHPECR...ESTLTVTFSQ → MTVDSSMSSG...RNAQSKHLSK

    Note: Initiator Met-1 is removed. Contains a N-acetylthreonine at position 2.

    Show »
    Length:265
    Mass (Da):30,359
    Checksum:i66AD5D84EFA6D6CB
    GO
    Isoform 3 (identifier: Q8WWW0-3) [UniParc]FASTAAdd to Basket

    Also known as: C, NORE1B

    The sequence of this isoform differs from the canonical sequence as follows:
         331-336: LFQKLS → GCLLHP
         337-418: Missing.

    Show »
    Length:336
    Mass (Da):37,433
    Checksum:i2657B6DAECD8D6A9
    GO

    Sequence cautioni

    The sequence AAH04270.1 differs from that shown. Reason: Aberrant splicing.
    The sequence AAH07203.1 differs from that shown. Reason: Aberrant splicing.
    The sequence AAH04270.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH07203.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 153153Missing in isoform 2. 5 PublicationsVSP_019363Add
    BLAST
    Alternative sequencei154 – 19340CKFTC…VTFSQ → MTVDSSMSSGYCSLDEELED CFFTAKTTFFRNAQSKHLSK in isoform 2. 5 PublicationsVSP_019364Add
    BLAST
    Alternative sequencei331 – 3366LFQKLS → GCLLHP in isoform 3. 1 PublicationVSP_019365
    Alternative sequencei337 – 41882Missing in isoform 3. 1 PublicationVSP_019366Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF445801 mRNA. Translation: AAL38592.1.
    AY261332 mRNA. Translation: AAP83360.1.
    AY062002 mRNA. Translation: AAL40388.1.
    AY062003 mRNA. Translation: AAL40389.1.
    AY216268 mRNA. Translation: AAO61668.1.
    AK289861 mRNA. Translation: BAF82550.1.
    AL832784 mRNA. Translation: CAI46164.1.
    AL591846, AL354681 Genomic DNA. Translation: CAI13536.1.
    AL591846, AL354681 Genomic DNA. Translation: CAI13538.1.
    AL354681, AL591846 Genomic DNA. Translation: CAI15252.1.
    AL591846, AL354681 Genomic DNA. Translation: CAI13537.1.
    AL591846, AL354681 Genomic DNA. Translation: CAI13542.1.
    AL354681, AL591846 Genomic DNA. Translation: CAI15253.1.
    AL354681, AL591846 Genomic DNA. Translation: CAI15254.1.
    AL354681, AL591846 Genomic DNA. Translation: CAI15256.1.
    CH471100 Genomic DNA. Translation: EAW93544.1.
    BC004270 mRNA. Translation: AAH04270.1. Sequence problems.
    BC007203 mRNA. Translation: AAH07203.1. Sequence problems.
    BC042651 mRNA. Translation: AAH42651.1.
    CCDSiCCDS1463.1. [Q8WWW0-3]
    CCDS1464.1. [Q8WWW0-2]
    CCDS30998.1. [Q8WWW0-1]
    RefSeqiNP_872604.1. NM_182663.3. [Q8WWW0-1]
    NP_872605.1. NM_182664.3. [Q8WWW0-3]
    NP_872606.1. NM_182665.3. [Q8WWW0-2]
    UniGeneiHs.497579.

    Genome annotation databases

    EnsembliENST00000577571; ENSP00000462576; ENSG00000266094. [Q8WWW0-2]
    ENST00000579436; ENSP00000462099; ENSG00000266094. [Q8WWW0-1]
    ENST00000580449; ENSP00000462544; ENSG00000266094. [Q8WWW0-3]
    GeneIDi83593.
    KEGGihsa:83593.
    UCSCiuc001hed.3. human. [Q8WWW0-1]
    uc001hee.3. human. [Q8WWW0-3]
    uc001hef.3. human. [Q8WWW0-2]

    Polymorphism databases

    DMDMi74751587.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF445801 mRNA. Translation: AAL38592.1 .
    AY261332 mRNA. Translation: AAP83360.1 .
    AY062002 mRNA. Translation: AAL40388.1 .
    AY062003 mRNA. Translation: AAL40389.1 .
    AY216268 mRNA. Translation: AAO61668.1 .
    AK289861 mRNA. Translation: BAF82550.1 .
    AL832784 mRNA. Translation: CAI46164.1 .
    AL591846 , AL354681 Genomic DNA. Translation: CAI13536.1 .
    AL591846 , AL354681 Genomic DNA. Translation: CAI13538.1 .
    AL354681 , AL591846 Genomic DNA. Translation: CAI15252.1 .
    AL591846 , AL354681 Genomic DNA. Translation: CAI13537.1 .
    AL591846 , AL354681 Genomic DNA. Translation: CAI13542.1 .
    AL354681 , AL591846 Genomic DNA. Translation: CAI15253.1 .
    AL354681 , AL591846 Genomic DNA. Translation: CAI15254.1 .
    AL354681 , AL591846 Genomic DNA. Translation: CAI15256.1 .
    CH471100 Genomic DNA. Translation: EAW93544.1 .
    BC004270 mRNA. Translation: AAH04270.1 . Sequence problems.
    BC007203 mRNA. Translation: AAH07203.1 . Sequence problems.
    BC042651 mRNA. Translation: AAH42651.1 .
    CCDSi CCDS1463.1. [Q8WWW0-3 ]
    CCDS1464.1. [Q8WWW0-2 ]
    CCDS30998.1. [Q8WWW0-1 ]
    RefSeqi NP_872604.1. NM_182663.3. [Q8WWW0-1 ]
    NP_872605.1. NM_182664.3. [Q8WWW0-3 ]
    NP_872606.1. NM_182665.3. [Q8WWW0-2 ]
    UniGenei Hs.497579.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4LGD X-ray 3.05 E/F/G/H 365-413 [» ]
    ProteinModelPortali Q8WWW0.
    SMRi Q8WWW0. Positions 113-170, 205-362, 366-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123689. 29 interactions.
    DIPi DIP-32490N.
    IntActi Q8WWW0. 30 interactions.
    STRINGi 9606.ENSP00000347443.

    PTM databases

    PhosphoSitei Q8WWW0.

    Polymorphism databases

    DMDMi 74751587.

    Proteomic databases

    MaxQBi Q8WWW0.
    PaxDbi Q8WWW0.
    PRIDEi Q8WWW0.

    Protocols and materials databases

    DNASUi 83593.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000577571 ; ENSP00000462576 ; ENSG00000266094 . [Q8WWW0-2 ]
    ENST00000579436 ; ENSP00000462099 ; ENSG00000266094 . [Q8WWW0-1 ]
    ENST00000580449 ; ENSP00000462544 ; ENSG00000266094 . [Q8WWW0-3 ]
    GeneIDi 83593.
    KEGGi hsa:83593.
    UCSCi uc001hed.3. human. [Q8WWW0-1 ]
    uc001hee.3. human. [Q8WWW0-3 ]
    uc001hef.3. human. [Q8WWW0-2 ]

    Organism-specific databases

    CTDi 83593.
    GeneCardsi GC01P206680.
    HGNCi HGNC:17609. RASSF5.
    HPAi CAB022664.
    MIMi 607020. gene.
    neXtProti NX_Q8WWW0.
    PharmGKBi PA134958571.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG308852.
    HOGENOMi HOG000013025.
    HOVERGENi HBG054362.
    InParanoidi Q8WWW0.
    KOi K08015.
    OMAi NCLLMKL.
    OrthoDBi EOG7TF796.
    PhylomeDBi Q8WWW0.
    TreeFami TF319243.

    Enzyme and pathway databases

    SignaLinki Q8WWW0.

    Miscellaneous databases

    GeneWikii RASSF5.
    GenomeRNAii 83593.
    NextBioi 72517.
    PROi Q8WWW0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WWW0.
    Bgeei Q8WWW0.
    CleanExi HS_RASSF5.
    Genevestigatori Q8WWW0.

    Family and domain databases

    InterProi IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000159. Ras-assoc.
    IPR011524. SARAH_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00130. C1_1. 1 hit.
    PF00788. RA. 1 hit.
    [Graphical view ]
    SMARTi SM00109. C1. 1 hit.
    SM00314. RA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50200. RA. 1 hit.
    PS50951. SARAH. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RASSF3 and NORE1: identification and cloning of two human homologues of the putative tumor suppressor gene RASSF1."
      Tommasi S., Dammann R., Jin S.-G., Zhang X.-F., Avruch J., Pfeifer G.P.
      Oncogene 21:2713-2720(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    2. "RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1."
      Katagiri K., Maeda A., Shimonaka M., Kinashi T.
      Nat. Immunol. 4:741-748(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN INTEGRIN ACTIVATION, INTERACTION WITH RAP1A AND ITGAL, SUBCELLULAR LOCATION.
    3. "RASSF3 is regulated by methylation in lung and breast tumor cell lines."
      Burbee D.G., White M.A., Minna J.D.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lymph node.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Skin.
    9. "The pro-apoptotic Ras effector Nore1 may serve as a Ras-regulated tumor suppressor in the lung."
      Vos M.D., Martinez A., Ellis C.A., Vallecorsa T., Clark G.J.
      J. Biol. Chem. 278:21938-21943(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A TUMOR SUPPRESSOR, TISSUE SPECIFICITY.
    10. "Regulation of the MST1 kinase by autophosphorylation, by the growth inhibitory proteins, RASSF1 and NORE1, and by Ras."
      Praskova M., Khoklatchev A., Ortiz-Vega S., Avruch J.
      Biochem. J. 381:453-462(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STK4/MST1.
    11. "Local activation of Rap1 contributes to directional vascular endothelial cell migration accompanied by extension of microtubules on which RAPL, a Rap1-associating molecule, localizes."
      Fujita H., Fukuhara S., Sakurai A., Yamagishi A., Kamioka Y., Nakaoka Y., Masuda M., Mochizuki N.
      J. Biol. Chem. 280:5022-5031(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MICROTUBULE GROWTH REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH RAP1A.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRASF5_HUMAN
    AccessioniPrimary (citable) accession number: Q8WWW0
    Secondary accession number(s): A8K1E6
    , Q5SY32, Q8WWV9, Q8WXF4, Q9BT99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3